Development of a macromolecular diffraction resource at CHESS, the Cornell High Energy Synchrotron Source will be continued. This resource devises novel x-ray diffraction techniques and apparatus, suitable for the study of macromolecules and macrmolecular assemblies such as enzymes, hormones, immunoglobulins, membranes and membrane components, DNA and DNA-protein complexes, ribosomes, and plant, insect and mammalian viruses, in the form of single crystals, fibers, membranes and solutions. Techniques exploit the unique features of a synchrotron x-ray source: its intensity, its polychromatic nature, and its time structure. The Laue technique for time-resolved crystallography will be developed further using both a new focussed white beam line and a high energy undulator; novel x-ray optical components will be devised; a new form of sensitive, low noise x-ray detector, the Kodak storage phosphor detector, will be evaluated; and an x-ray wiggler beam line optimized for macromolecular crystallography, especially of viruses, will be installed. The last will be incorporated into a Biohazards Facility suitable for handling concentrated solutions and crystals of Pathogenic viruses at the BL3 level in the NIH/CDC classification. To our knowledge, it will be unique in the world. These facilities will continue to be made widely available to scientists from university, government and industry who are interested in macromolecular diffraction as a probe of structure and function.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR001646-07
Application #
3103974
Study Section
(SSS)
Project Start
1983-09-01
Project End
1993-08-31
Budget Start
1989-09-01
Budget End
1990-08-31
Support Year
7
Fiscal Year
1989
Total Cost
Indirect Cost
Name
Cornell University
Department
Type
Schools of Arts and Sciences
DUNS #
City
Ithaca
State
NY
Country
United States
Zip Code
14850
Kozlov, Guennadi; Wong, Kathy; Gehring, Kalle (2018) Crystal structure of the Legionella effector Lem22. Proteins 86:263-267
Ménade, Marie; Kozlov, Guennadi; Trempe, Jean-François et al. (2018) Structures of ubiquitin-like (Ubl) and Hsp90-like domains of sacsin provide insight into pathological mutations. J Biol Chem 293:12832-12842
Xu, Jie; Kozlov, Guennadi; McPherson, Peter S et al. (2018) A PH-like domain of the Rab12 guanine nucleotide exchange factor DENND3 binds actin and is required for autophagy. J Biol Chem 293:4566-4574
Dean, Dexter N; Rana, Pratip; Campbell, Ryan P et al. (2018) Propagation of an A? Dodecamer Strain Involves a Three-Step Mechanism and a Key Intermediate. Biophys J 114:539-549
Chen, Yu Seby; Kozlov, Guennadi; Fakih, Rayan et al. (2018) The cyclic nucleotide-binding homology domain of the integral membrane protein CNNM mediates dimerization and is required for Mg2+ efflux activity. J Biol Chem 293:19998-20007
Lucido, Michael J; Orlando, Benjamin J; Vecchio, Alex J et al. (2016) Crystal Structure of Aspirin-Acetylated Human Cyclooxygenase-2: Insight into the Formation of Products with Reversed Stereochemistry. Biochemistry 55:1226-38
Bauman, Joseph D; Harrison, Jerry Joe E K; Arnold, Eddy (2016) Rapid experimental SAD phasing and hot-spot identification with halogenated fragments. IUCrJ 3:51-60
Xu, Caishuang; Kozlov, Guennadi; Wong, Kathy et al. (2016) Crystal Structure of the Salmonella Typhimurium Effector GtgE. PLoS One 11:e0166643
Cogliati, Massimo; Zani, Alberto; Rickerts, Volker et al. (2016) Multilocus sequence typing analysis reveals that Cryptococcus neoformans var. neoformans is a recombinant population. Fungal Genet Biol 87:22-9
Oot, Rebecca A; Kane, Patricia M; Berry, Edward A et al. (2016) Crystal structure of yeast V1-ATPase in the autoinhibited state. EMBO J 35:1694-706

Showing the most recent 10 out of 375 publications